ID A0A0V1CYN7_TRIBR Unreviewed; 431 AA.
AC A0A0V1CYN7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
DE AltName: Full=Phenylalanyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031194};
DE Flags: Fragment;
GN Name=Fars2 {ECO:0000313|EMBL:KRY54328.1};
GN ORFNames=T03_16732 {ECO:0000313|EMBL:KRY54328.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY54328.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY54328.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY54328.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) +
CC L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668,
CC Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20;
CC Evidence={ECO:0000256|ARBA:ARBA00000395};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY54328.1}.
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DR EMBL; JYDI01000071; KRY54328.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1CYN7; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00496; PheRS_alpha_core; 1.
DR Gene3D; 3.30.70.380; Ferrodoxin-fold anticodon-binding domain; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR005121; Fdx_antiC-bd.
DR InterPro; IPR036690; Fdx_antiC-bd_sf.
DR InterPro; IPR004530; Phe-tRNA-synth_IIc_mito.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR NCBIfam; TIGR00469; pheS_mito; 1.
DR PANTHER; PTHR11538:SF41; PHENYLALANINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF03147; FDX-ACB; 1.
DR Pfam; PF01409; tRNA-synt_2d; 2.
DR SMART; SM00896; FDX-ACB; 1.
DR SUPFAM; SSF54991; Anticodon-binding domain of PheRS; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51447; FDX_ACB; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:KRY54328.1};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 153..336
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT DOMAIN 338..431
FT /note="FDX-ACB"
FT /evidence="ECO:0000259|PROSITE:PS51447"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY54328.1"
SQ SEQUENCE 431 AA; 50155 MW; A9B326BC93047FC2 CRC64;
LVQQTTEMFN RRYIKNAYKQ FCLSSSLLEQ NCSPEFCVDS FTNVKQSILA LVGRKLHRCP
DSPLYILKRR IFDYFNLNYK TSTGRSLYAI FDNFDPIVSK WQNFDSLLVP SDHICRSPSD
TYYLNSHQLL RTHTSAHQNE LIASGLRHFL IVGDVYRRDQ VDCNHYPCFH QLEGVHLFAD
YQLFQPDIVD QCDLFEKGIR NYEKQETHTL ECVTLVGKHL KQCLESMVTY LLSAEGKKVQ
MRWVKAYFPF THPSWELEIL YRDNWIEILG CGVIEQKILE NAGTGDLVGW AFGIGLERLA
MQLFEIPDIR IFWSKDSGIL SQFAVADYNA NIKFKPISRY PQCSNDISFW LADSNSFSDT
DFYDLVRSVG GDVVEQVNRI DEFVHPKTKK KSICYRITYR HMERTLTQEE VNVIHSAIAE
NAHKELGVIV R
//
